-
1
-
-
0037551741
-
Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
-
DOI 10.1146/annurev.neuro.26.010302.081142
-
B. Caughey, and P.T. Lansbury Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders Annu. Rev. Neurosci. 26 2003 267 298 (Pubitemid 37064935)
-
(2003)
Annual Review of Neuroscience
, vol.26
, pp. 267-298
-
-
Caughey, B.1
Lansbury Jr., P.T.2
-
2
-
-
33746377894
-
Protein misfolding, functional amyloid, and human disease
-
DOI 10.1146/annurev.biochem.75.101304.123901
-
F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
-
(2006)
Annual Review of Biochemistry
, vol.75
, pp. 333-366
-
-
Chiti, F.1
Dobson, C.M.2
-
3
-
-
78349247103
-
Prion amyloid structure explains templating: How proteins can be genes
-
R.B. Wickner, and F. Shewmaker C.L. Winchester Prion amyloid structure explains templating: how proteins can be genes FEMS Yeast Res. 10 2010 980 991
-
(2010)
FEMS Yeast Res.
, vol.10
, pp. 980-991
-
-
Wickner, R.B.1
Shewmaker, F.2
Winchester, C.L.3
-
4
-
-
77957782470
-
Biology of amyloid: Structure, function, and regulation
-
J. Greenwald, and R. Riek Biology of amyloid: structure, function, and regulation Structure 18 2010 1244 1260
-
(2010)
Structure
, vol.18
, pp. 1244-1260
-
-
Greenwald, J.1
Riek, R.2
-
5
-
-
0031592945
-
Common core structure of amyloid fibrils by synchrotron X-ray diffraction
-
DOI 10.1006/jmbi.1997.1348
-
M. Sunde, and L.C. Serpell C.C. Blake Common core structure of amyloid fibrils by synchrotron x-ray diffraction J. Mol. Biol. 273 1997 729 739 (Pubitemid 27488813)
-
(1997)
Journal of Molecular Biology
, vol.273
, Issue.3
, pp. 729-739
-
-
Sunde, M.1
Serpell, L.C.2
Bartlam, M.3
Fraser, P.E.4
Pepys, M.B.5
Blake, C.C.F.6
-
6
-
-
0028800177
-
Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
-
H.H. Bauer, and U. Aebi H.P. Merkle Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin J. Struct. Biol. 115 1995 1 15
-
(1995)
J. Struct. Biol.
, vol.115
, pp. 1-15
-
-
Bauer, H.H.1
Aebimerkle, H.P.U.2
-
7
-
-
24044507958
-
Multiple assembly pathways underlie amyloid-β fibril polymorphisms
-
DOI 10.1016/j.jmb.2005.07.029, PII S002228360500817X
-
C. Goldsbury, and P. Frey S.A. Müller Multiple assembly pathways underlie amyloid-beta fibril polymorphisms J. Mol. Biol. 352 2005 282 298 (Pubitemid 41213315)
-
(2005)
Journal of Molecular Biology
, vol.352
, Issue.2
, pp. 282-298
-
-
Goldsbury, C.1
Frey, P.2
Olivieri, V.3
Aebi, U.4
Muller, S.A.5
-
8
-
-
23444445907
-
2-microglobulin into amyloid
-
DOI 10.1016/j.jmb.2005.06.040, PII S0022283605007023
-
W.S. Gosal, and I.J. Morten S.E. Radford Competing pathways determine fibril morphology in the self-assembly of β2-microglobulin into amyloid J. Mol. Biol. 351 2005 850 864 (Pubitemid 41111901)
-
(2005)
Journal of Molecular Biology
, vol.351
, Issue.4
, pp. 850-864
-
-
Gosal, W.S.1
Morten, I.J.2
Hewitt, E.W.3
Smith, D.A.4
Thomson, N.H.5
Radford, S.E.6
-
9
-
-
12244249201
-
Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
-
DOI 10.1126/science.1105850
-
A.T. Petkova, and R.D. Leapman R. Tycko Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils Science 307 2005 262 265 (Pubitemid 40116242)
-
(2005)
Science
, vol.307
, Issue.5707
, pp. 262-265
-
-
Petkova, A.T.1
Leapman, R.D.2
Guo, Z.3
Yau, W.-M.4
Mattson, M.P.5
Tycko, R.6
-
10
-
-
57349120654
-
Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and x-ray fiber diffraction
-
J. Madine, and E. Jack D.A. Middleton Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and x-ray fiber diffraction J. Am. Chem. Soc. 130 2008 14990 15001
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 14990-15001
-
-
Madine, J.1
Jackmiddleton, D.A.E.2
-
11
-
-
79952971653
-
Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability
-
K.E. Marshall, and K.L. Morris L.C. Serpell Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability Biochemistry 50 2011 2061 2071
-
(2011)
Biochemistry
, vol.50
, pp. 2061-2071
-
-
Marshall, K.E.1
Morris, K.L.2
Serpell, L.C.3
-
12
-
-
34249290108
-
Atomic structures of amyloid cross-β spines reveal varied steric zippers
-
DOI 10.1038/nature05695, PII NATURE05695
-
M.R. Sawaya, and S. Sambashivan D. Eisenberg Atomic structures of amyloid cross-β spines reveal varied steric zippers Nature 447 2007 453 457 (Pubitemid 46816731)
-
(2007)
Nature
, vol.447
, Issue.7143
, pp. 453-457
-
-
Sawaya, M.R.1
Sambashivan, S.2
Nelson, R.3
Ivanova, M.I.4
Sievers, S.A.5
Apostol, M.I.6
Thompson, M.J.7
Balbirnie, M.8
Wiltzius, J.J.W.9
McFarlane, H.T.10
Madsen, A.O.11
Riekel, C.12
Eisenberg, D.13
-
13
-
-
79955896407
-
The amyloid formation mechanism in human IAPP: Dimers have β-strand monomer-monomer interfaces
-
N.F. Dupuis, and C. Wu M.T. Bowers The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces J. Am. Chem. Soc. 133 2011 7240 7243
-
(2011)
J. Am. Chem. Soc.
, vol.133
, pp. 7240-7243
-
-
Dupuis, N.F.1
Wubowers, M.T.C.2
-
14
-
-
79953183597
-
Atomic structures suggest determinants of transmission barriers in mammalian prion disease
-
M.I. Apostol, and J.J. Wiltzius D. Eisenberg Atomic structures suggest determinants of transmission barriers in mammalian prion disease Biochemistry 50 2011 2456 2463
-
(2011)
Biochemistry
, vol.50
, pp. 2456-2463
-
-
Apostol, M.I.1
Wiltziuseisenberg, D.J.J.2
-
15
-
-
79953245314
-
Amyloid structure: Conformational diversity and consequences
-
B.H. Toyama, and J.S. Weissman Amyloid structure: conformational diversity and consequences Annu. Rev. Biochem. 80 2011 557 585
-
(2011)
Annu. Rev. Biochem.
, vol.80
, pp. 557-585
-
-
Toyama, B.H.1
Weissman, J.S.2
-
17
-
-
78751685655
-
What drives amyloid molecules to assemble into oligomers and fibrils?
-
J.D. Schmit, K. Ghosh, and K. Dill What drives amyloid molecules to assemble into oligomers and fibrils? Biophys. J. 100 2011 450 458
-
(2011)
Biophys. J.
, vol.100
, pp. 450-458
-
-
Schmit, J.D.1
Ghosh, K.2
Dill, K.3
-
18
-
-
73649140576
-
The common architecture of cross-β amyloid
-
T.R. Jahn, and O.S. Makin L.C. Serpell The common architecture of cross-β amyloid J. Mol. Biol. 395 2010 717 727
-
(2010)
J. Mol. Biol.
, vol.395
, pp. 717-727
-
-
Jahn, T.R.1
Makin, O.S.2
Serpell, L.C.3
-
19
-
-
20444440728
-
Structure of the cross-β spine of amyloid-like fibrils
-
DOI 10.1038/nature03680
-
R. Nelson, and M.R. Sawaya D. Eisenberg Structure of the cross-β spine of amyloid-like fibrils Nature 435 2005 773 778 (Pubitemid 40839722)
-
(2005)
Nature
, vol.435
, Issue.7043
, pp. 773-778
-
-
Nelson, R.1
Sawaya, M.R.2
Balbirnie, M.3
Madsen, A.O.4
Riekel, C.5
Grothe, R.6
Eisenberg, D.7
-
20
-
-
0037168655
-
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
-
DOI 10.1073/pnas.262663499
-
A.T. Petkova, and Y. Ishii R. Tycko A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR Proc. Natl. Acad. Sci. USA 99 2002 16742 16747 (Pubitemid 36034043)
-
(2002)
Proceedings of the National Academy of Sciences of the United States of America
, vol.99
, Issue.26
, pp. 16742-16747
-
-
Petkova, A.T.1
Ishii, Y.2
Balbach, J.J.3
Antzutkin, O.N.4
Leapman, R.D.5
Delaglio, F.6
Tycko, R.7
-
21
-
-
79952099447
-
Fluoroalcohol-induced modulation of the pathway of amyloid protofibril formation by barstar
-
A. Sekhar, and J.B. Udgaonkar Fluoroalcohol-induced modulation of the pathway of amyloid protofibril formation by barstar Biochemistry 50 2011 805 819
-
(2011)
Biochemistry
, vol.50
, pp. 805-819
-
-
Sekhar, A.1
Udgaonkar, J.B.2
-
22
-
-
0033520461
-
Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
-
D.M. Walsh, and D.M. Hartley D.B. Teplow Amyloid β-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates J. Biol. Chem. 274 1999 25945 25952
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 25945-25952
-
-
Walsh, D.M.1
Hartley, D.M.2
Teplow, D.B.3
-
24
-
-
77956138054
-
Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein
-
S. Jain, and J.B. Udgaonkar Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein Biochemistry 49 2010 7615 7624
-
(2010)
Biochemistry
, vol.49
, pp. 7615-7624
-
-
Jain, S.1
Udgaonkar, J.B.2
-
25
-
-
67650079178
-
Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein
-
S. Kumar, and J.B. Udgaonkar Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein Biochemistry 48 2009 6441 6449
-
(2009)
Biochemistry
, vol.48
, pp. 6441-6449
-
-
Kumar, S.1
Udgaonkar, J.B.2
-
26
-
-
58149400915
-
Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation
-
S. Kumar, and J.B. Udgaonkar Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation J. Mol. Biol. 385 2009 1266 1276
-
(2009)
J. Mol. Biol.
, vol.385
, pp. 1266-1276
-
-
Kumar, S.1
Udgaonkar, J.B.2
-
27
-
-
75349097530
-
A causative link between the structure of aberrant protein oligomers and their toxicity
-
S. Campioni, and B. Mannini F. Chiti A causative link between the structure of aberrant protein oligomers and their toxicity Nat. Chem. Biol. 6 2010 140 147
-
(2010)
Nat. Chem. Biol.
, vol.6
, pp. 140-147
-
-
Campioni, S.1
Manninichiti, F.B.2
-
28
-
-
36849084640
-
Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid
-
DOI 10.1038/nsmb1345, PII NSMB1345
-
S. Chimon, and M.A. Shaibat Y. Ishii Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid Nat. Struct. Mol. Biol. 14 2007 1157 1164 (Pubitemid 350223342)
-
(2007)
Nature Structural and Molecular Biology
, vol.14
, Issue.12
, pp. 1157-1164
-
-
Chimon, S.1
Shaibat, M.A.2
Jones, C.R.3
Calero, D.C.4
Aizezi, B.5
Ishii, Y.6
-
29
-
-
0034869176
-
Protofibrils, the unifying toxic molecule of neurodegenerative disorders?
-
DOI 10.1038/nn0901-859
-
C. Haass, and H. Steiner Protofibrils, the unifying toxic molecule of neurodegenerative disorders? Nat. Neurosci. 4 2001 859 860 (Pubitemid 32801582)
-
(2001)
Nature Neuroscience
, vol.4
, Issue.9
, pp. 859-860
-
-
Haass, C.1
Steiner, H.2
-
30
-
-
0037102362
-
Getting out of shape
-
C.M. Dobson Getting out of shape Nature 418 2002 729 730
-
(2002)
Nature
, vol.418
, pp. 729-730
-
-
Dobson, C.M.1
-
31
-
-
2342569618
-
Conformational constraints for amyloid fibrillation: The importance of being unfolded
-
DOI 10.1016/j.bbapap.2003.12.008, PII S1570963904000020
-
V.N. Uversky, and A.L. Fink Conformational constraints for amyloid fibrillation: the importance of being unfolded Biochim. Biophys. Acta 1698 2004 131 153 (Pubitemid 38591469)
-
(2004)
Biochimica et Biophysica Acta - Proteins and Proteomics
, vol.1698
, Issue.2
, pp. 131-153
-
-
Uversky, V.N.1
Fink, A.L.2
-
32
-
-
70350134740
-
Characterization of the heterogeneity and specificity of interpolypeptide interactions in amyloid protofibrils by measurement of site-specific fluorescence anisotropy decay kinetics
-
A. Jha, J.B. Udgaonkar, and G. Krishnamoorthy Characterization of the heterogeneity and specificity of interpolypeptide interactions in amyloid protofibrils by measurement of site-specific fluorescence anisotropy decay kinetics J. Mol. Biol. 393 2009 735 752
-
(2009)
J. Mol. Biol.
, vol.393
, pp. 735-752
-
-
Jha, A.1
Udgaonkar, J.B.2
Krishnamoorthy, G.3
-
33
-
-
33745039756
-
Characterization of the Formation of Amyloid Protofibrils from Barstar by Mapping Residue-specific Fluorescence Dynamics
-
DOI 10.1016/j.jmb.2006.02.006, PII S0022283606001744
-
S. Mukhopadhyay, and P.K. Nayak G. Krishnamoorthy Characterization of the formation of amyloid protofibrils from barstar by mapping residue-specific fluorescence dynamics J. Mol. Biol. 358 2006 935 942 (Pubitemid 44382447)
-
(2006)
Journal of Molecular Biology
, vol.358
, Issue.4
, pp. 935-942
-
-
Mukhopadhyay, S.1
Nayak, P.K.2
Udgaonkar, J.B.3
Krishnamoorthy, G.4
-
34
-
-
0037031291
-
NMR identification and characterization of the flexible regions in the 160 kDA molten globule-like aggregate of barstar at low pH
-
DOI 10.1021/bi026034w
-
J. Juneja, and N.S. Bhavesh R.V. Hosur NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH Biochemistry 41 2002 9885 9899 (Pubitemid 34839736)
-
(2002)
Biochemistry
, vol.41
, Issue.31
, pp. 9885-9899
-
-
Juneja, J.1
Bhavesh, N.S.2
Udgaonkar, J.B.3
Hosur, R.V.4
-
35
-
-
0346102546
-
Effect of environmental conditions on aggregation and fibril formation of barstar
-
DOI 10.1007/s00249-003-0336-5
-
K. Gast, and A.J. Modler G. Damaschun Effect of environmental conditions on aggregation and fibril formation of barstar Eur. Biophys. J. 32 2003 710 723 (Pubitemid 38031358)
-
(2003)
European Biophysics Journal
, vol.32
, Issue.8
, pp. 710-723
-
-
Gast, K.1
Modler, A.J.2
Damaschun, H.3
Krober, R.4
Lutsch, G.5
Zirwer, D.6
Golbik, R.7
Damaschun, G.8
-
37
-
-
33847769109
-
Mechanism of Formation of Amyloid Protofibrils of Barstar from Soluble Oligomers: Evidence for Multiple Steps and Lateral Association Coupled to Conformational Conversion
-
DOI 10.1016/j.jmb.2007.01.039, PII S0022283607000794
-
S. Kumar, S.K. Mohanty, and J.B. Udgaonkar Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion J. Mol. Biol. 367 2007 1186 1204 (Pubitemid 46389623)
-
(2007)
Journal of Molecular Biology
, vol.367
, Issue.4
, pp. 1186-1204
-
-
Kumar, S.1
Mohanty, S.K.2
Udgaonkar, J.B.3
-
39
-
-
0033571653
-
Sidechain interactions in parallel β sheets: The energetics of cross- strand pairings
-
DOI 10.1016/S0969-2126(00)80023-4
-
J.S. Merkel, J.M. Sturtevant, and L. Regan Sidechain interactions in parallel β sheets: the energetics of cross-strand pairings Structure 7 1999 1333 1343 (Pubitemid 29529874)
-
(1999)
Structure
, vol.7
, Issue.11
, pp. 1333-1343
-
-
Merkel, J.S.1
Sturtevant, J.M.2
Regan, L.3
-
40
-
-
30344445370
-
Amino acid pairing preferences in parallel β-sheets in proteins
-
DOI 10.1016/j.jmb.2005.11.008, PII S002228360501394X
-
H.M. Fooks, and A.C. Martin E.G. Hutchinson Amino acid pairing preferences in parallel beta-sheets in proteins J. Mol. Biol. 356 2006 32 44 (Pubitemid 43069725)
-
(2006)
Journal of Molecular Biology
, vol.356
, Issue.1
, pp. 32-44
-
-
Fooks, H.M.1
Martin, A.C.R.2
Woolfson, D.N.3
Sessions, R.B.4
Hutchinson, E.G.5
-
41
-
-
23244449092
-
Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p
-
DOI 10.1021/bi050724t
-
J.C. Chan, and N.A. Oyler R. Tycko Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p Biochemistry 44 2005 10669 10680 (Pubitemid 41098243)
-
(2005)
Biochemistry
, vol.44
, Issue.31
, pp. 10669-10680
-
-
Chan, J.C.C.1
Oyler, N.A.2
Yau, W.-M.3
Tycko, R.4
-
42
-
-
33845334180
-
2- microglobulin fragment probed by solid-state NMR
-
DOI 10.1073/pnas.0607180103
-
K. Iwata, and T. Fujiwara Y. Goto 3D structure of amyloid protofilaments of β2-microglobulin fragment probed by solid-state NMR Proc. Natl. Acad. Sci. USA 103 2006 18119 18124 (Pubitemid 44871622)
-
(2006)
Proceedings of the National Academy of Sciences of the United States of America
, vol.103
, Issue.48
, pp. 18119-18124
-
-
Iwata, K.1
Fujiwara, T.2
Matsuki, Y.3
Akutsu, H.4
Takahashi, S.5
Naiki, H.6
Goto, Y.7
-
43
-
-
37549063068
-
Role of intermolecular forces in defining material properties of protein nanofibrils
-
T.P. Knowles, and A.W. Fitzpatrick M.E. Welland Role of intermolecular forces in defining material properties of protein nanofibrils Science 318 2007 1900 1903
-
(2007)
Science
, vol.318
, pp. 1900-1903
-
-
Knowles, T.P.1
Fitzpatrick, A.W.2
Welland, M.E.3
-
45
-
-
0032444658
-
Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
-
DOI 10.1017/S003358359800345X
-
M. Buck Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins Q. Rev. Biophys. 31 1998 297 355 (Pubitemid 29213772)
-
(1998)
Quarterly Reviews of Biophysics
, vol.31
, Issue.3
, pp. 297-355
-
-
Buck, M.1
-
47
-
-
0028174643
-
Quantitative determination of helical propensities from trifluoroethanol titration curves
-
A. Jasanoff, and A.R. Fersht Quantitative determination of helical propensities from trifluoroethanol titration curves Biochemistry 33 1994 2129 2135
-
(1994)
Biochemistry
, vol.33
, pp. 2129-2135
-
-
Jasanoff, A.1
Fersht, A.R.2
-
48
-
-
0028301327
-
1 domain. Evidence of trifluoroethanol induced native-like β-hairpin formation
-
DOI 10.1021/bi00185a041
-
F.J. Blanco, and M.A. Jiménez J.L. Nieto NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like β-hairpin formation Biochemistry 33 1994 6004 6014 (Pubitemid 24184606)
-
(1994)
Biochemistry
, vol.33
, Issue.19
, pp. 6004-6014
-
-
Blanco, F.J.1
Jimenez, M.A.2
Pineda, A.3
Rico, M.4
Santoro, J.5
Nieto, J.L.6
-
49
-
-
0030593499
-
Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat
-
DOI 10.1006/jmbi.1996.0412
-
N. Schönbrunner, and J. Wey T. Kiefhaber Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat J. Mol. Biol. 260 1996 432 445 (Pubitemid 26254122)
-
(1996)
Journal of Molecular Biology
, vol.260
, Issue.3
, pp. 432-445
-
-
Schonbrunner, N.1
Josef, W.2
Engels, J.3
Georg, H.4
Kiefhaber, T.5
-
50
-
-
33748943122
-
2- Microglobulin Fragment Are Induced by Fluorine-substituted Alcohols
-
DOI 10.1016/j.jmb.2006.08.030, PII S0022283606010588
-
K. Yamaguchi, H. Naiki, and Y. Goto Mechanism by which the amyloid-like fibrils of a β2-microglobulin fragment are induced by fluorine-substituted alcohols J. Mol. Biol. 363 2006 279 288 (Pubitemid 44429956)
-
(2006)
Journal of Molecular Biology
, vol.363
, Issue.1
, pp. 279-288
-
-
Yamaguchi, K.-i.1
Naiki, H.2
Goto, Y.3
|